Tikhomirova N K, Kochetov G A
A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
Biochem Int. 1990 Oct;22(1):31-6.
Baker's yeast transketolase has been purified by immunoaffinity chromatography on specific TK antibodies covalently linked to CNBr-agarose. Affinity chromatography allows a 480-fold purification of TK from yeast extracts and about 80% recovery of the original activity. The isolated enzyme has a specific activity of 12-60 U/mg and during polyacrylamide gel electrophoresis performed at pH 8.9 migrates as two protein bands possessing a transketolase activity which corresponds to two isoforms of the enzyme.
通过在与溴化氰琼脂糖共价连接的特异性转酮醇酶（TK）抗体上进行免疫亲和层析，已纯化出面包酵母转酮醇酶。亲和层析可从酵母提取物中对TK进行480倍的纯化，并使原始活性回收率约为80%。分离出的酶的比活性为12 - 60 U/mg，在pH 8.9条件下进行的聚丙烯酰胺凝胶电泳中，以两条具有转酮醇酶活性的蛋白带形式迁移，这两条带对应于该酶的两种同工型。
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